6a67 - Revision history

OCA at 09:18, 22 November 2023

2023-11-22T09:18:59Z

← Older revision		Revision as of 09:18, 22 November 2023
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	<StructureSection load='6a67' size='340' side='right'caption='[[6a67]], [[Resolution\|resolution]] 2.33Å' scene=''>		<StructureSection load='6a67' size='340' side='right'caption='[[6a67]], [[Resolution\|resolution]] 2.33Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[6a67]] is a 6 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~] and [~~http~~://en.wikipedia.org/wiki/~~Influenza_a_virus_~~(a/~~thailand~~/1(~~kan~~-1)/2004(~~h5n1~~)) Influenza a virus (a/~~thailand~~/1(~~kan~~-1)/2004(~~h5n1~~))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A67 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=6A67 FirstGlance]. <br>		<table><tr><td colspan='2'>[[6a67]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/Thailand/1(KAN-1)/2004(H5N1)) Influenza A virus (A/Thailand/1(KAN-1)/2004(H5N1))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A67 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6A67 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>		</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.33Å</td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=6a67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a67 OCA], [~~http~~://pdbe.org/6a67 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6a67 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6a67 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6a67 ProSAT]</span></td></tr>		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
			<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6a67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a67 OCA], [https://pdbe.org/6a67 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6a67 RCSB], [https://www.ebi.ac.uk/pdbsum/6a67 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6a67 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[~~[http~~://www.uniprot.org/uniprot/Q6Q794_9INFA Q6Q794_9INFA]] Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization either through clathrin-dependent endocytosis or through clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.[SAAS:SAAS01039674] Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.[RuleBase:RU003324]		[https://www.uniprot.org/uniprot/Q6Q794_9INFA Q6Q794_9INFA] Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization either through clathrin-dependent endocytosis or through clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.[SAAS:SAAS01039674] Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.[RuleBase:RU003324]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Human~~]]		[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Sun, J]]		[[Category: Sun J]]
	[[Category: Wang, P]]		[[Category: Wang P]]
	[[Category: Wang, X]]		[[Category: Wang X]]
	[[Category: Zhang, L]]		[[Category: Zhang L]]
	[[Category: Zuo, Y]]		[[Category: Zuo Y]]
	~~[[Category: H5n1]]~~
	~~[[Category: Immune system]]~~
	~~[[Category: Influenza virus]]~~
	~~[[Category: Neutralizing antibody]]~~
	~~[[Category: Receptor binding site~~]]

OCA at 21:26, 28 October 2020

2020-10-28T21:26:49Z

← Older revision		Revision as of 21:26, 28 October 2020
Line 1:		Line 1:

	==Crystal structure of influenza A virus H5 hemagglutinin globular head in complex with the Fab of antibody FLD21.140==		==Crystal structure of influenza A virus H5 hemagglutinin globular head in complex with the Fab of antibody FLD21.140==
	<StructureSection load='6a67' size='340' side='right' caption='[[6a67]], [[Resolution\|resolution]] 2.33Å' scene=''>		<StructureSection load='6a67' size='340' side='right'caption='[[6a67]], [[Resolution\|resolution]] 2.33Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[6a67]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Influenza_a_virus_(a/thailand/1(kan-1)/2004(h5n1)) Influenza a virus (a/thailand/1(kan-1)/2004(h5n1))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A67 OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6A67 FirstGlance]. <br>		<table><tr><td colspan='2'>[[6a67]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Influenza_a_virus_(a/thailand/1(kan-1)/2004(h5n1)) Influenza a virus (a/thailand/1(kan-1)/2004(h5n1))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A67 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6A67 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://~~oca.weizmann.ac~~.~~il/oca-docs~~/fgij/fg.htm?mol=6a67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a67 OCA], [http://pdbe.org/6a67 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a67 RCSB], [http://www.ebi.ac.uk/pdbsum/6a67 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a67 ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6a67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a67 OCA], [http://pdbe.org/6a67 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a67 RCSB], [http://www.ebi.ac.uk/pdbsum/6a67 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a67 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	</div>		</div>
	<div class="pdbe-citations 6a67" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 6a67" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[Hemagglutinin 3D structures\|Hemagglutinin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 23:		Line 26:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
			[[Category: Large Structures]]
	[[Category: Sun, J]]		[[Category: Sun, J]]
	[[Category: Wang, P]]		[[Category: Wang, P]]

OCA at 20:15, 19 September 2018

2018-09-19T20:15:24Z

← Older revision		Revision as of 20:15, 19 September 2018
Line 3:		Line 3:
	<StructureSection load='6a67' size='340' side='right' caption='[[6a67]], [[Resolution\|resolution]] 2.33Å' scene=''>		<StructureSection load='6a67' size='340' side='right' caption='[[6a67]], [[Resolution\|resolution]] 2.33Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[6a67]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A67 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6A67 FirstGlance]. <br>		<table><tr><td colspan='2'>[[6a67]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Influenza_a_virus_(a/thailand/1(kan-1)/2004(h5n1)) Influenza a virus (a/thailand/1(kan-1)/2004(h5n1))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A67 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6A67 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6a67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a67 OCA], [http://pdbe.org/6a67 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a67 RCSB], [http://www.ebi.ac.uk/pdbsum/6a67 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a67 ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6a67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a67 OCA], [http://pdbe.org/6a67 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a67 RCSB], [http://www.ebi.ac.uk/pdbsum/6a67 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a67 ProSAT]</span></td></tr>
Line 9:		Line 9:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/Q6Q794_9INFA Q6Q794_9INFA]] Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization either through clathrin-dependent endocytosis or through clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.[SAAS:SAAS01039674] Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.[RuleBase:RU003324]		[[http://www.uniprot.org/uniprot/Q6Q794_9INFA Q6Q794_9INFA]] Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization either through clathrin-dependent endocytosis or through clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.[SAAS:SAAS01039674] Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.[RuleBase:RU003324]
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			The highly pathogenic avian influenza virus H5N1 is a major threat to global public health and therefore a high-priority target of current vaccine development. The receptor-binding site (RBS) on the globular head of hemagglutinin (HA) in the viral envelope is one of the major target sites for antibody recognition against H5N1 and other influenza viruses. Here, we report the identification and characterization of a pair of human RBS-specific antibodies, designated FLD21.140 and AVFluIgG03, that are mutually complementary in their neutralizing activities against a diverse panel of H5N1 viruses. Crystallographic analysis and site-directed mutagenesis revealed that the two antibodies share a similar RBS-binding mode and their individual specificities are governed by residues at positions 133a, 144, and 145. Specifically, FLD21.140 preferred Leu-133a/Lys-144/Ser-145, whereas AVFluIgG03 favored Ser-133a /Thr-144/Pro-145 residue triplets, both of which perfectly matched the most prevalent residues in viruses from epidemic-originating regions. Of note, according to an analysis of 3758 H5 HAs sequences available in the Influenza Virus Database at the National Center for Biotechnology Information, the residues Leu-133a/Ser-133a and Ser-145/Pro-145 constituted more than 87.6% and 99.3% of all residues at these two positions, respectively. Taken together, our results provide a structural understanding for the neutralizing complementarity of these two antibodies and improve our understanding of the RBS-specific antibody response against H5N1 infection in humans.

			Complementary recognition of the receptor binding site of highly pathogenic H5N1 influenza viruses by two human neutralizing antibodies.,Zuo Y, Wang P, Sun J, Guo S, Wang G, Zuo T, Fan S, Zhou P, Liang M, Shi X, Wang X, Zhang L J Biol Chem. 2018 Aug 28. pii: RA118.004604. doi: 10.1074/jbc.RA118.004604. PMID:30154240<ref>PMID:30154240</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 6a67" style="background-color:#fffaf0;"></div>
			== References ==
			<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Human]]
	[[Category: Sun, J]]		[[Category: Sun, J]]
	[[Category: Wang, P]]		[[Category: Wang, P]]

OCA at 07:23, 29 August 2018

2018-08-29T07:23:33Z

@@ Line 1: / Line 1: @@
-The entry 6a67 is ON HOLD
+==Crystal structure of influenza A virus H5 hemagglutinin globular head in complex with the Fab of antibody FLD21.140==
+<StructureSection load='6a67' size='340' side='right' caption='[[6a67]], [[Resolution|resolution]] 2.33&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6a67]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A67 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6A67 FirstGlance]. <br>
-Description:
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-[[Category: Unreleased Structures]]
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6a67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a67 OCA], [http://pdbe.org/6a67 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a67 RCSB], [http://www.ebi.ac.uk/pdbsum/6a67 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a67 ProSAT]</span></td></tr>

OCA: Protected "6a67" [edit=sysop:move=sysop]

2018-07-04T05:33:38Z

Protected "6a67" [edit=sysop:move=sysop]

← Older revision	Revision as of 05:33, 4 July 2018
(No difference)

OCA: New page: '''Unreleased structure''' The entry 6a67 is ON HOLD Authors: Description: Category: Unreleased Structures

2018-07-04T05:33:37Z

New page: '''Unreleased structure''' The entry 6a67 is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 6a67 is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]